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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
purine-specific nucleoside hydrolase, inosine nucleosidase, inosine hydrolase, inosine-adenosine-guanosine nucleoside hydrolase, guanosine-inosine-preferring nucleoside n-ribohydrolase,
more
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guanosine-inosine-preferring nucleoside N-ribohydrolase
-
-
inosine-adenosine-guanosine nucleoside hydrolase
inosine-guanosine nucleosidase
-
-
-
-
nucleosidase, inosine
-
-
-
-
purine-specific nucleoside hydrolase
-
inosine-adenosine-guanosine nucleoside hydrolase
-
purine-specific
inosine-adenosine-guanosine nucleoside hydrolase
-
purine-specific
-
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inosine + H2O = D-ribose + hypoxanthine
-
-
-
-
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hydrolysis of N-glycosyl bond
-
-
-
-
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1-methylguanosine + H2O
1-methylguanine + D-ribose
-
-
-
-
?
1-N2-ethenoguanosine + H2O
1-N2-ethenoguanine + D-ribose
-
-
-
-
?
1-N2-isopropenoguanosine + H2O
1-N2-isopropenoguanine + D-ribose
-
-
-
-
?
5-methyluridine + H2O
D-ribose + 5-methyluracil
-
-
-
-
?
6-mercaptopurine riboside + H2O
6-mercaptopurine + D-ribose
7-methylguanosine + H2O
7-methylguanine + D-ribose
-
-
-
-
?
8-azainosine + H2O
8-azahypoxanthine + D-ribose
-
-
-
-
?
adenosine + H2O
adenine + D-ribose
adenosine + H2O
D-ribose + adenine
guanosine + H2O
D-ribose + guanine
guanosine + H2O
guanine + D-ribose
inosine + H2O
D-ribose + hypoxanthine
inosine + H2O
hypoxanthine + D-ribose
purine riboside + H2O
purine + D-ribose
-
nebularine
-
?
uridine + H2O
D-ribose + uracil
-
-
-
-
?
xanthosine + H2O
D-ribose + xanthine
-
-
-
-
?
xanthosine + H2O
xanthine + D-ribose
additional information
?
-
6-mercaptopurine riboside + H2O
6-mercaptopurine + D-ribose
-
inhibitor and substrate
-
-
?
6-mercaptopurine riboside + H2O
6-mercaptopurine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
-
?
adenosine + H2O
adenine + D-ribose
-
-
-
-
?
adenosine + H2O
D-ribose + adenine
-
-
-
-
?
adenosine + H2O
D-ribose + adenine
-
after 1 h, the rate of adenosine cleavage is about 12.5%
-
-
?
adenosine + H2O
D-ribose + adenine
-
after 1 h, the rate of adenosine cleavage is about 12.5%
-
-
?
guanosine + H2O
D-ribose + guanine
-
after 1 h, the rate of guanosine cleavage is about 16%
-
-
?
guanosine + H2O
D-ribose + guanine
-
after 1 h, the rate of guanosine cleavage is about 16%
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
guanosine is hydrolyzed 12% faster than inosine
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
-
?
guanosine + H2O
guanine + D-ribose
-
-
-
-
?
inosine + H2O
D-ribose + hypoxanthine
-
-
-
-
?
inosine + H2O
D-ribose + hypoxanthine
-
isoform NSH2 shows highest hydrolysis capacity for inosine
-
-
?
inosine + H2O
D-ribose + hypoxanthine
-
best substrate
-
-
?
inosine + H2O
D-ribose + hypoxanthine
-
best substrate
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
guanosine is hydrolyzed 12% faster than inosine
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
-
?
xanthosine + H2O
xanthine + D-ribose
-
-
-
-
?
xanthosine + H2O
xanthine + D-ribose
-
-
-
-
?
xanthosine + H2O
xanthine + D-ribose
-
-
-
-
?
additional information
?
-
-
the pure recombinant protein exhibits highest hydrolase activity for uridine, followed by inosine and adenosine
-
-
?
additional information
?
-
-
adenosine and xanthosine are poor substrates. No substrate are: 2'-deoxyguanosine, 2'-deoxyinosine, 2'-methylguanosine, pyrimidine nucleosides and 5'-GMP
-
-
?
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inosine + H2O
hypoxanthine + D-ribose
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
inosine + H2O
hypoxanthine + D-ribose
-
-
-
?
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Ca2+
-
up to 6fold activation by exogenous CaCl2 or Ca(NO3)2
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2'-deoxyguanosine
-
competitive
2'-methylguanosine
-
competitive
6-mercaptopurine riboside
-
-
ATP
-
binds to I1- and I2-site, noncompetitive inhibition, ligand exclusion model
Co2+
-
24.2% residual activity at 0.1 M using inosine as substrate, 25.8% residual activity at 0.1 M using guanosine as substrate, 33.3% residual activity at 0.1 M using adenosine as substrate
Cu2+
-
10.6% residual activity at 0.1 M using inosine as substrate, 9.67% residual activity at 0.1 M using guanosine as substrate, complete inhibition at 0.1 M using adenosine as substrate
Fe2+
-
60.6% residual activity at 0.1 M using inosine as substrate, 54.8% residual activity at 0.1 M using guanosine as substrate, 66.6% residual activity at 0.1 M using adenosine as substrate
Mg2+
-
62.1% residual activity at 0.1 M using inosine as substrate, 74.2% residual activity at 0.1 M using guanosine as substrate, 75% residual activity at 0.1 M using adenosine as substrate
NaCN
-
60.6% residual activity at 0.1 M using inosine as substrate, 38.7% residual activity at 0.1 M using guanosine as substrate, 41.6% residual activity at 0.1 M using adenosine as substrate
nucleoside diphosphates
-
less effective inhibitor compared to nucleoside triphosphates, non competitive inhibition
nucleoside monophosphates
-
slight inhibition or no effect
nucleoside triphosphates
-
most potent inhibitor, non competitive inhibition
Theobromine
-
at alkaline pH
adenine
-
binds to I2-site; partial noncompetitive
adenine
-
partial noncompetitive
hypoxanthine
-
binds to I2-site; partial noncompetitive
hypoxanthine
-
partial noncompetitive
Mn2+
-
-
Mn2+
-
complete inhibition at 0.1 M using inosine, adenosine or guanosine as substrate
Zn2+
-
-
Zn2+
-
57.5% residual activity at 0.1 M using inosine as substrate, 45.2% residual activity at 0.1 M using guanosine as substrate, 41.6% residual activity at 0.1 M using adenosine as substrate
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Infections
Structures of purine nucleosidase from Trypanosoma brucei bound to isozyme-specific trypanocidals and a novel metalorganic inhibitor.
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0.44
methyluridine
-
pH and temperature not specified in the publication
0.8
uridine
-
pH and temperature not specified in the publication
additional information
additional information
-
kinetics
-
0.06
adenosine
-
-
0.7
adenosine
-
pH and temperature not specified in the publication
0.0027
guanosine
-
pH 4.8
0.0025
Inosine
-
-
1.4
Inosine
-
recombinant enzyme expressed in Escherichia coli
1.4
Inosine
-
pH and temperature not specified in the publication
1.2
Xanthosine
-
pH 7.1
1.69
Xanthosine
-
pH and temperature not specified in the publication
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23.3
Inosine
-
-
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0.0015
2'-deoxyguanosine
Lupinus luteus
-
pH 4.8
0.0036
2'-methylguanosine
Lupinus luteus
-
pH 4.8
0.021
adenosine
Lupinus luteus
-
pH 4.8
0.0097
guanine
Lupinus luteus
-
pH 4.8
0.06
Mn2+
Lupinus luteus
-
pH 4.8
0.06
Zn2+
Lupinus luteus
-
pH 4.8
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0.00275
-
substrate: inosine
14.5
-
purified recombinant enzyme, substrate inosine
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7
-
substrate: xanthosine
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9
-
no xanthosine hydrolysis above this temperature
9
-
50% of the optimum value
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105 - 115
-
105°C: maximal activity, 115°C: 50% of maximal activity
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-
-
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brenda
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-
-
brenda
-
-
-
brenda
subsp. Kurstaki
UniProt
brenda
-
-
-
brenda
Jerusalem artichoke
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
ecotype Columbia
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-
brenda
-
-
-
brenda
L. cv. Topaz
-
-
brenda
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-
5fold increase in activity during seed germination
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
of roots and in root tips
brenda
-
-
brenda
-
-
-
brenda
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-
-
brenda
-
-
brenda
-
-
brenda
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physiological function
-
isoform NSH2 acts during the late phase of senescence and supports inosine breakdown
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URH1_ARATH
336
0
36086
Swiss-Prot
other Location (Reliability: 2 )
URH2_ARATH
322
0
34668
Swiss-Prot
other Location (Reliability: 2 )
NSH3_ARATH
890
0
99072
Swiss-Prot
Secretory Pathway (Reliability: 1 )
IUNH_CRIFA
315
0
34326
Swiss-Prot
other Location (Reliability: 3 )
IUNH_LEIMA
314
0
34310
Swiss-Prot
other Location (Reliability: 2 )
A0A2G9FXT6_9LAMI
320
0
34258
TrEMBL
other Location (Reliability: 2 )
A0A396JQD2_MEDTR
339
0
36337
TrEMBL
other Location (Reliability: 1 )
A0A7S7M5C6_LEIDO
312
0
33980
TrEMBL
other Location (Reliability: 2 )
A0A7S7M5D0_LEIDO
312
0
34010
TrEMBL
other Location (Reliability: 2 )
A0A7S7RT38_LEIDO
312
0
34011
TrEMBL
other Location (Reliability: 3 )
B7FJZ5_MEDTR
322
0
34322
TrEMBL
other Location (Reliability: 2 )
A0A7S7M5D6_LEIDO
312
0
34077
TrEMBL
other Location (Reliability: 2 )
A0A2P6RHV4_ROSCH
322
0
34392
TrEMBL
other Location (Reliability: 1 )
A0A7S7RT81_LEIDO
312
0
33984
TrEMBL
other Location (Reliability: 3 )
A0A7S7M6Z8_LEIDO
312
0
34050
TrEMBL
other Location (Reliability: 2 )
A7UHH1_BACTK
321
0
36271
TrEMBL
-
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34000
-
2 * 34000 Da, SDS-PAGE, predicted: 34325 Da/subunit, intersubunit disulfide bond
70000
-
gel filtration
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monomer
-
1 * 80000, SDS-PAGE
homodimer
-
2 * 34000 Da, SDS-PAGE, predicted: 34325 Da/subunit, intersubunit disulfide bond
homodimer
-
2 * 34000 Da, SDS-PAGE, predicted: 34325 Da/subunit, intersubunit disulfide bond
-
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additional information
-
mutants expressing the Arabidopsis thaliana enzyme or the homologue from Oryza sativa exhibit resistance toward toxic fluorouridine, fluorouracil, and fluoroorotic acid. Mutants with increased and decreased nucleosidase activity are delayed in germination
additional information
-
mutant strains lacking the basal layer protein exsY and devoid of exosporium lack detectable levels of collagen-like glycoprotein BclA and the basal layer proteins BxpB, BxpC, CotY, and inosine-uridine-preferring nucleoside hydrolase. The mutation does not affect spore production and germination efficiencies or spore resistance but does influence the course of spore outgrow
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50 - 60
-
the enzyme shows 68.18%, 45.45% and 28.78% residual activities for inosine hydrolysis after 4 min, 6 min, and 8 min of incubation, respectively, at 50°C. The enzyme is completely inactivated after 10 min at 50°C and 4 min at 60°C
90
-
100% activity after 1h, apparent melting temperature: 107°C
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hydrolysis activity for inosine, guanosine and adenosine is highest in citrate-phosphate buffer
-
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-20°C, tolerates repeated freeze-thawing
-
-25°C, highly stable at deep-freeze conditions
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-5°C, in citrate-phosphate buffer (pH 4.0), the enzyme retains 100%, 95.7%, 93,6% and 82.9% activity for inosine hydrolysis after 24 h, 48 h, 72 h and 120 h of incubation, respectively
-
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highly purified, 233fold
-
-
-
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URH1, DNA and amino acid sequence determination and analysis, expression in Escherichia coli, functional complementation of a yeast mutant, expression in transgenic Arabidopsis thaliana mutant plants under control of the CaMV 35S promoter
-
-
-
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Yoshino, M.; Tsukada, T.
A kinetic study of inosine nucleosidase from Azotobacter vinelandii
Int. J. Biochem.
20
971-975
1988
Azotobacter vinelandii
-
brenda
Guranowski, A.
Purine catabolism in plants
Plant Physiol.
70
344-349
1982
Lupinus luteus
brenda
Le Floc'h, F.; Lafleuriel, J.
The purine nucleosidases of Jerusalem artichoke shoots
Phytochemistry
20
2127-2129
1981
Helianthus tuberosus
-
brenda
Yoshino, M.; Tsukada, T.; Tsushima, K.
Inosine nucleosidase from Azotobacter vinelandii. Purification and properties
Arch. Microbiol.
119
59-64
1978
Azotobacter vinelandii, Azotobacter vinelandii 0
brenda
Koch, A.L.
Some enzymes of nucleoside metabolism of Escherichia coli
J. Biol. Chem.
223
535-549
1956
Escherichia coli
brenda
Redmond, C.; Baillie, L.W.J.; Hibbs, S.; Moir, A.J.G.; Moir, A.
Identification of proteins in the exosporium of Bacillus anthracis
Microbiology
150
355-363
2004
Bacillus anthracis
brenda
Boydston, J.A.; Yue, L.; Kearney, J.F.; Turnbough, C.L.
The ExsY protein is required for complete formation of the exosporium of Bacillus anthracis
J. Bacteriol.
188
7440-7448
2006
Bacillus anthracis
brenda
Szuwart, M.; Starzynska, E.; Pietrowska-Borek, M.; Guranowski, A.
Calcium-stimulated guanosine--inosine nucleosidase from yellow lupin (Lupinus luteus)
Phytochemistry
67
1476-1485
2006
Lupinus luteus
brenda
Porcelli, M.; Peluso, I.; Marabotti, A.; Facchiano, A.; Cacciapuoti, G.
Biochemical characterization and homology modeling of a purine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus: insights into mechanisms of protein stabilization
Arch. Biochem. Biophys.
483
55-65
2009
Saccharolobus solfataricus, Saccharolobus solfataricus P2
brenda
Liang, L.; He, X.; Liu, G.; Tan, H.
The role of a purine-specific nucleoside hydrolase in spore germination of Bacillus thuringiensis
Microbiology
154
1333-1340
2008
Bacillus thuringiensis (A7UHH1), Bacillus thuringiensis
brenda
Jung, B.; Floerchinger, M.; Kunz, H.H.; Traub, M.; Wartenberg, R.; Jeblick, W.; Neuhaus, H.E.; Moehlmann, T.
Uridine-ribohydrolase is a key regulator in the uridine degradation pathway of Arabidopsis
Plant Cell
21
876-891
2009
Arabidopsis thaliana
brenda
Mach, J.
Uridine ribohydrolase and the balance between nucleotide degradation and salvage
Plant Cell
21
699
2009
Arabidopsis thaliana
brenda
Elshafei, A.; Mohamed, L.; Hassan, M.
Degradation of purine ribonucleosides by extracts of Penicillium viridicatum
Afr. J. Microbiol. Res.
5
316-323
2011
Penicillium viridicatum, Penicillium viridicatum NRC 3712
-
brenda
Jung, B.; Hoffmann, C.; Moehlmann, T.
Arabidopsis nucleoside hydrolases involved in intracellular and extracellular degradation of purines
Plant J.
65
703-711
2011
Arabidopsis thaliana
brenda
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